Modulation of Catalysis and Inhibition of Fetal Bovine Serum Acetylcholinesteraseby Monoclonal Antibodies

摘要

Monoclonal antibodies have been raised against acetyicholinesterase isolated froma variety of sources and species. Although none of these antibodies bind to the esteratic site, some of them appear to interact with the region of the catalytic subunit referred to as the peripheral anionic site. We describe here the production and characterization of six inhibitory monoclonal antibodies against fetal bovine serum acetylcholinesterase. Results show that changes in the conformation of acetyicholinesterase caused by interaction with monoclonal antibodies at a site remote from the catalytic site result in the modulation of catalytic activity of acetylcholinesterase.